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J Biol Chem, Vol. 274, Issue 29, 20664-20670, July 16, 1999

Apoptosis Promotes a Caspase-induced Amino-terminal Truncation of Ikappa Balpha That Functions as a Stable Inhibitor of NF-kappa B

Julie Y. Reuther and Albert S. Baldwin Jr.§

From the Lineberger Comprehensive Cancer Center, Curriculum in Genetics and Molecular Biology, and § Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599-7295

Caspases are cell death cysteine proteases that are activated upon the induction of the apoptotic program and cleave target proteins in a sequence-specific manner to promote cell death. Recently, Barkett et al. (Barkett, M., Xue, D., Horvitz, H. R., and Gilmore, T. D. (1997) J. Biol. Chem. 272, 29419-29422) have shown that Ikappa Balpha , the inhibitory subunit of the transcription factor NF-kappa B, can be cleaved by caspase-3 in vitro at a site that potentially produces a dominant inhibitory form of Ikappa Balpha . The involvement of NF-kappa B in the inhibition of cell death led us to ask whether apoptotic stimuli would induce the caspase-mediated cleavage of Ikappa Balpha in vivo. In this study, we show that apoptosis leads to the caspase-mediated amino-terminal truncation of Ikappa Balpha (Delta N-Ikappa Balpha ). Our data show that Delta N-Ikappa Balpha can bind NF-kappa B, suppress NF-kappa B activation, and sensitize cells to death. Since activated NF-kappa B plays a role in the inhibition of cell death, these data suggest that caspase-mediated cleavage of Ikappa Balpha may be a mechanism to suppress NF-kappa B and its associated antiapoptotic activity.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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